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Merck
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重要文件

SML2490

Sigma-Aldrich

APC366 trifluoroacetate

≥97% (HPLC)

同義詞:

APC 366 trifluoroacetate, N-(1-Hydroxy-2-naphthoyl)-L-arginyl-L-prolinamide, N2-[(1-Hydroxy-2-naphthalenyl)carbonyl]-L-arginyl-L-prolinamide trifluoroacetate

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About This Item

經驗公式(希爾表示法):
C22H28N6O4 · xC2HF3O2
CAS號碼:
分子量::
440.50 (free base basis)
分類程式碼代碼:
12352200
NACRES:
NA.77
暫時無法取得訂價和供貨情況

化驗

≥97% (HPLC)

形狀

lyophilized powder

顏色

white to off-white

運輸包裝

wet ice

儲存溫度

−20°C

SMILES 字串

FC(F)(C(O)=O)F.NC(NCCC[C@@H](C(N1CCC[C@H]1C(N)=O)=O)NC(C2=C(O)C3=CC=CC=C3C=C2)=O)=N

InChI

1S/C22H28N6O4/c23-19(30)17-8-4-12-28(17)21(32)16(7-3-11-26-22(24)25)27-20(31)15-10-9-13-5-1-2-6-14(13)18(15)29/h1-2,5-6,9-10,16-17,29H,3-4,7-8,11-12H2,(H2,23,30)(H,27,31)(H4,24,25,26)/t16-,17-/m0/s1

InChI 密鑰

SKYWIMYOGAWOMB-IRXDYDNUSA-N

生化/生理作用

APC366 is a selective inhibitor of mast cell tryptase, which is involved with allergenic response. It thereby also inhibits protease-activated receptor PAR2, a G-protein-coupled receptor that is activated by mast cell tryptase. Tryptase has been proposed to be involved in fibrosis, joint inflammation and also in promoting breast cancer angiogenesis, all of which APC366 inhibited.
Mast cell tryptase inhibitor

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分析證明 (COA)

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Neng Qian et al.
Oncology letters, 16(2), 1513-1520 (2018-07-17)
Mast cells have been demonstrated to accumulate around and within solid tumors of numerous types, and express a number of pro-angiogenic compounds, including tryptase. They may serve an early role in angiogenesis within developing tumors. In the present study, the
Issan Yee San Tam et al.
International archives of allergy and immunology, 177(3), 199-206 (2018-07-19)
Mast cells are key immune effector cells which release chemokines, proteases, and other inflammatory mediators upon activation by immunological stimuli. The aim of this study was to investigate the effects of co-releasing proteases on the kinetics of release of the
Alexandre Denadai-Souza et al.
Arthritis research & therapy, 19(1), 124-124 (2017-06-08)
Increasing evidences indicate that an unbalance between tryptases and their endogenous inhibitors, leading to an increased proteolytic activity, is implicated in the pathophysiology of rheumatoid arthritis. The aim of the present study was to evaluate the impact of tryptase inhibition

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